|BS||Biotechnology||Nanjing University||Nanjing, China|
|PhD||Biochemistry||University of Maryland, Baltimore County||Baltimore, Md.|
NMR investigations of RNA structures and virus:host interactions in HIV-1 replication.
The main research interest in our lab is to understand the structure of viral RNA and the structural basis of virus:host interactions to begin to decipher the mechanism of HIV-1 viral replication.
DHX9 / RNA helicase A (RHA) is a host factor that influences HIV-1 replication in many steps. It co-assembles with viral RNA genome to support viral infectivity. We recently reported that the RHA recruitment during virus assembly is mediated by the interactions between the N-terminal domain of RHA and the RNA elements near the primer binding site (PBS) in the 5′-UTR of the viral RNA genome. A variety of biophysical techniques including NMR spectroscopy, small angle X-ray scattering and isothermal titration calorimetry are employed to study the RNA structural elements important for RHA recruitment. We are also investigating the function of RHA during reverse transcription to unraveling its role during the early replication steps.
Notable Honors and Service
Dr. Richard Wallace Faculty Incentive Grant Award (University of Missouri, Columbia), 2014
Career Transition Award, Center for HIV RNA Studies (CRNA), 2013
Brady S, Singh G, Bolinger C, Song Z, Boeras I, Weng K, Trent B, Brown WC, Singh K, Boris-Lawrie K, Heng X. (2019). Virion-associated, host-derived DHX9/RNA helicase A enhances the processivity of HIV-1 reverse transcriptase on genomic RNA. J Biol Chem. 294(30):11473-11485. doi: 10.1074/jbc.RA119.007679. [PubMed]
Zhang K, Keane SC, Su Z, Irobalieva RN, Chen M, Van V, Sciandra CA, Marchant J, Heng X, Schmid MF, Case DA, Ludtke SJ, Summers MF, Chiu W. (2018). Structure of the 30 kDa HIV-1 RNA Dimerization Signal by a Hybrid Cryo-EM, NMR, and Molecular Dynamics Approach. Structure. 26(3):490-498.e3. doi: 10.1016/j.str.2018.01.001. [PubMed]
Sun LZ, Heng X, Chen SJ. (2017). Theory Meets Experiment: Metal Ion Effects in HCV Genomic RNA Kissing Complex Formation. Front Mol Biosci. 4:92. doi: 10.3389/fmolb.2017.00092. eCollection 2017. Review. [PubMed]
Naorem SS, Han J, Wang S, Lee WR, Heng X, Miller JF, Guo H. (2017). DGR mutagenic transposition occurs via hypermutagenic reverse transcription primed by nicked template RNA. Proc Natl Acad Sci U S A. 114(47):E10187-E10195. doi: 10.1073/pnas.1715952114. [PubMed]
Kranawetter C, Brady S, Sun L, Schroeder M, Chen SJ, Heng X. (2017). Nuclear Magnetic Resonance Study of RNA Structures at the 3′-End of the Hepatitis C Virus Genome. Biochemistry. 56(37):4972-4984. doi: 10.1021/acs.biochem.7b00573. [PubMed]
Boeras I, Seufzer B, Brady S, Rendahl A, Heng X, Boris-Lawrie K. (2017). The basal translation rate of authentic HIV-1 RNA is regulated by 5’UTR nt-pairings at junction of R and U5. Sci Rep. 7(1):6902. doi: 10.1038/s41598-017-06883-9. [PubMed]
Keane SC, Van V, Frank HM, Sciandra CA, McCowin S, Santos J, Heng X, Summers MF. (2016). NMR detection of intermolecular interaction sites in the dimeric 5′-leader of the HIV-1 genome. Proc Natl Acad Sci U S A. 113(46):13033-13038. [PubMed]
Boeras I, Song Z, Moran A, Franklin J, Brown WC, Johnson M, Boris-Lawrie K, Heng X. (2016). DHX9/RHA Binding to the PBS-Segment of the Genomic RNA during HIV-1 Assembly Bolsters Virion Infectivity. J Mol Biol. 428(11):2418-2429. doi: 10.1016/j.jmb.2016.04.011. [PubMed]
NIH R01AI150460, Structural basis of the HIV-1 PBS-segment mediated RHA recruitment during assembly to bolster virus infectivity